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1lsp
From Proteopedia
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THE CRYSTAL STRUCTURE OF A BULGECIN-INHIBITED G-TYPE LYSOZYME FROM THE EGG-WHITE OF THE AUSTRALIAN BLACK SWAN. A COMPARISON OF THE BINDING OF BULGECIN TO THREE MURAMIDASES
Overview
Bulgecin A, a bacterial metabolite, has been shown to bind in the, active-site groove of the chicken-type lysozyme from the rainbow trout, (RBTL) and in the lysozyme-like C-terminal domain, of a soluble lytic, transglycosylase (C-SLT) from Escherichia coli. These enzymes are, muramidases that cleave the glycosidic bonds in the glycan strands of the, murein polymer. Here we report the crystal structure of a complex between, the goose-type lysozyme from the egg white of the Australian black swan, (SEWL) and bulgecin A at 2.45 A resolution. As is the case for the, C-SLT/bulgecin and RBTL/bulgecin complexes, the ligand binds with the, N-acetylglucosamine ring in subsite C and the proline moiety in site D, where it interacts with the catalytic glutamic acid. The taurine residue, interacts with the beta-sheet region. Comparisons of the three buigecin, complexes show that the inhibitor has the same binding mode to the, muramidases with similar protein-ligand interactions, particularly for, SEWL and RBTL. From our results, it seems likely that bulgecin, in, general, inhibits enzymes with lysozyme-like domains and thus might, represent a novel class of natural antibiotics that act on, murein-degrading rather than murein-synthesizing enzymes.
About this Structure
1LSP is a Single protein structure of sequence from Cygnus atratus with BUL as ligand. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
Structure of a bulgecin-inhibited g-type lysozyme from the egg white of the Australian black swan. A comparison of the binding of bulgecin to three muramidases., Karlsen S, Hough E, Rao ZH, Isaacs NW, Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):105-14. PMID:15299731
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